نتایج جستجو برای: phosphoenolpyruvate carboxylase pepc

تعداد نتایج: 10363  

Journal: :Plant physiology 2015
Jianghua Shi Keke Yi Yu Liu Li Xie Zhongjing Zhou Yue Chen Zhanghua Hu Tao Zheng Renhu Liu Yunlong Chen Jinqing Chen

Phosphoenolpyruvate carboxylase (PEPC) is a crucial enzyme that catalyzes an irreversible primary metabolic reaction in plants.Previous studies have used transgenic plants expressing ectopic PEPC forms with diminished feedback inhibition to examine the role of PEPC in carbon and nitrogen metabolism. To date, the in vivo role of PEPC in carbon and nitrogen metabolism has not been analyzed in pla...

Journal: :Plant physiology 1992
B Sugiharto T Sugiyama

We previously showed that the selective accumulation of phosphoenolpyruvate carboxylase (PEPC) in photosynthetically maturing maize (Zea mays L.) leaf cells induced by nitrate supply to nitrogen-starved plants was primarily a consequence of the level of its mRNA (B Sugiharto, K Miyata, H Nakamoto, H Sasakawa, T Sugiyama [1990] Plant Physiol 92: 963-969). To determine the specificity of inorgani...

Journal: :Horticulturae 2023

‘Xiangjiao’ plum (Prunus salicina Lindl.) is a stone fruit that vulnerable to the chilling injury (CI) caused by low-temperature stress. The effects of 1-methylcyclopropene (1-MCP) and ethylene absorbent (EA) treatments on quality malic acid metabolism stored at 4 °C were compared in this study. Compared with control check (CK) EA treatment, fumigation 1.0 mg·L−1 1-MCP for 24 h could more signi...

Journal: :The Plant journal : for cell and molecular biology 2007
Sam Gennidakis Srinath Rao Katie Greenham R Glen Uhrig Brendan O'Leary Wayne A Snedden Chaofu Lu William C Plaxton

Two classes of phosphoenolpyruvate carboxylase (PEPC) sharing the same 107-kDa catalytic subunit (p107) were previously purified from developing castor oil seed (COS) endosperm. The association of p107 with an immunologically unrelated 64-kDa polypeptide (p64) causes pronounced physical and kinetic differences between the Class-1 PEPC p107 homotetramer and Class-2 PEPC p107/p64 hetero-octamer. ...

Journal: :The Biochemical journal 2011
Brendan O'Leary Joonho Park William C Plaxton

PEPC [PEP (phosphoenolpyruvate) carboxylase] is a tightly controlled enzyme located at the core of plant C-metabolism that catalyses the irreversible β-carboxylation of PEP to form oxaloacetate and Pi. The critical role of PEPC in assimilating atmospheric CO(2) during C(4) and Crassulacean acid metabolism photosynthesis has been studied extensively. PEPC also fulfils a broad spectrum of non-pho...

Journal: :Journal of experimental botany 2003
Jhadeswar Murmu Bhaskarrao Chinthapalli Agepati S Raghavendra

The effect of Pi on the properties of phosphoenolpyruvate carboxylase (PEPC) from Amaranthus hypochondriacus, a NAD-ME type C4 plant, was studied in leaf extracts as well as with purified protein. Efforts were also made to modulate the Pi status of the leaf by feeding leaves with either Pi or mannose. Inclusion of 30 mM Pi during the assay enhanced the enzyme activity in leaf extracts or of pur...

Journal: :The Biochemical journal 1998
J Rivoal W C Plaxton D H Turpin

Phosphoenolpyruvate carboxylase (PEPC) is a key enzyme in the supply of carbon skeletons for the assimilation of nitrogen by green algae. Two PEPC isoforms with respective native molecular masses of 400 (PEPC1) and 650 (PEPC2) kDa have been purified from Chlamydomonas reinhardtii CW-15 cc1883 (Chlorophyceae). SDS/PAGE, immunoblot and CNBr peptide-mapping analyses indicate the presence of the sa...

2014
Bhaskarrao Chinthapalli D. S. Vijaya Chitra Agepati S. Raghavendra

Temperature caused marked modulation of phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) in leaf discs of Alternanthera pungens (C4 plant) as well as Lycopersicon esculentum (C3 species). The optimal incubation temperature for PEPC activity in A. pungens was 45 °C compared to 30 °C in L. esculentum. A. pungens lost nearly 61% of PEPC activity on exposure to a low temperature of 15 °C, compar...

2011
Brendan O'Leary Srinath K. Rao William C. Plaxton

PEPC [PEP (phosphoenolpyruvate) carboxylase] is a tightly controlled anaplerotic enzyme situated at a pivotal branch point of plant carbohydrate metabolism. Two distinct oligomeric PEPC classes were discovered in developing COS (castor oil seeds). Class-1 PEPC is a typical homotetramer of 107 kDa PTPC (plant-type PEPC) subunits, whereas the novel 910-kDa Class-2 PEPC hetero-octamer arises from ...

2009
Allison L. Gregory Brenden A. Hurley Hue T. Tran Alexander J. Valentine Yi-Min She Vicki L. Knowles William C. Plaxton

PEPC [PEP(phosphoenolpyruvate) carboxylase] is a tightly controlled cytosolic enzyme situated at a major branchpoint in plant metabolism. Accumulating evidence indicates important functions for PEPC and PPCK (PEPC kinase) in plant acclimation to nutritional P(i) deprivation. However, little is known about the genetic origin or phosphorylation status of native PEPCs from -P(i) (P(i)-deficient) p...

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